STE3_YEAST - dbPTM
STE3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STE3_YEAST
UniProt AC P06783
Protein Name Pheromone a factor receptor
Gene Name STE3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 470
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Receptor for the peptide pheromone a factor..
Protein Sequence MSYKSAIIGLCLLAVILLAPPLAWHSHTKNIPAIILITWLLTMNLTCIVDAAIWSDDDFLTRWDGKGWCDIVIKLQVGANIGISCAVTNIIYNLHTILKADSVLPDLSSWTKIVKDLVISLFTPVMVMGFSYLLQVFRYGIARYNGCQNLLSPTWITTVLYTMWMLIWSFVGAVYATLVLFVFYKKRKDVRDILHCTNSGLNLTRFARLLIFCFIIILVMFPFSVYTFVQDLQQVEGHYTFKNTHSSTIWNTIIKFDPGRPIYNIWLYVLMSYLVFLIFGLGSDALHMYSKFLRSIKLGFVLDMWKRFIDKNKEKRVGILLNKLSSRKESRNPFSTDSENYISTCTENYSPCVGTPISQAHFYVDYRIPDDPRKSQNKSKKYLFADKETDDILDEIDLKESRHIPYVTQGQSFDDEISLGGFSKVTLDYSEKLHNSASSNFEGESLCYSPASKEENSSSNEHSSENTAGP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
108PhosphorylationDSVLPDLSSWTKIVK
CCCCCCHHHHHHHHH
31.0721440633
111PhosphorylationLPDLSSWTKIVKDLV
CCCHHHHHHHHHHHH
16.9121440633
323AcetylationRVGILLNKLSSRKES
HHHHHHHHHHCCCHH
50.1124489116
323UbiquitinationRVGILLNKLSSRKES
HHHHHHHHHHCCCHH
50.1124961812
375PhosphorylationIPDDPRKSQNKSKKY
CCCCCCCCCCCCCCE
40.0225005228
387UbiquitinationKKYLFADKETDDILD
CCEEECCCCCCCCHH
60.1124961812
399UbiquitinationILDEIDLKESRHIPY
CHHHCCCCHHCCCCE
50.3124961812
408PhosphorylationSRHIPYVTQGQSFDD
HCCCCEECCCCCCCC
22.5730377154
412PhosphorylationPYVTQGQSFDDEISL
CEECCCCCCCCCCCC
37.1521440633
418PhosphorylationQSFDDEISLGGFSKV
CCCCCCCCCCCCEEE
20.9321440633
424UbiquitinationISLGGFSKVTLDYSE
CCCCCCEEEEEECHH
36.66-
426PhosphorylationLGGFSKVTLDYSEKL
CCCCEEEEEECHHHH
20.0421440633
430PhosphorylationSKVTLDYSEKLHNSA
EEEEEECHHHHHCCC
28.1125521595
432UbiquitinationVTLDYSEKLHNSASS
EEEECHHHHHCCCCC
49.45-
436PhosphorylationYSEKLHNSASSNFEG
CHHHHHCCCCCCCCC
20.8420377248
438PhosphorylationEKLHNSASSNFEGES
HHHHCCCCCCCCCCC
26.1520377248
439PhosphorylationKLHNSASSNFEGESL
HHHCCCCCCCCCCCC
45.3020377248
445PhosphorylationSSNFEGESLCYSPAS
CCCCCCCCCCCCCCC
34.3020377248
449PhosphorylationEGESLCYSPASKEEN
CCCCCCCCCCCCCCC
17.0021551504
452PhosphorylationSLCYSPASKEENSSS
CCCCCCCCCCCCCCC
43.9420377248
453UbiquitinationLCYSPASKEENSSSN
CCCCCCCCCCCCCCC
71.76-
458PhosphorylationASKEENSSSNEHSSE
CCCCCCCCCCCCCCC
49.0821551504
464PhosphorylationSSSNEHSSENTAGP-
CCCCCCCCCCCCCC-
36.4528889911

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of STE3_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STE3_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of STE3_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AKR1_YEASTAKR1physical
9243510
GBB_YEASTSTE4genetic
2104659
RCC1_YEASTSRM1genetic
2548085
ASG7_YEASTASG7genetic
11073982
STE20_YEASTSTE20genetic
8754848
PEX15_YEASTPEX15physical
16093310

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STE3_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430, AND MASSSPECTROMETRY.

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